Butyrylcholinesterase: Difference between revisions
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<StructureSection load='1p0m' size='450' side='right' scene= caption='Glycosylated human butyrylcholinesterase complex with choline, glycerol, sulfate and Cl- ions (PDB code 1p0m)'> | <StructureSection load='1p0m' size='450' side='right' scene= caption='Glycosylated human butyrylcholinesterase complex with choline, glycerol, sulfate and Cl- ions (PDB code 1p0m)'> | ||
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BChE biological role remains obscure, but mutations in the human BCHE gene result in prolonged post-surgical apnea due to the inability of the mutant BChEs to hydrolyse the local anaesthetic, succinylcholine. | BChE biological role remains obscure, but mutations in the human BCHE gene result in prolonged post-surgical apnea due to the inability of the mutant BChEs to hydrolyse the local anaesthetic, succinylcholine. | ||
== Structural highlights == | |||
Like in the AChE structure, BChE active site is located at the bottom of a ca. 20A deep gorge. The active site of BChE is similar to that of AChE. The differences are noticed in the lining of the gorge were some of the aromatic residues in AChE are substituted by hydrophobic ones and in the active site acyl-binding pocket where 2 Phe residues are replaced by Leu and Val in BChE. | |||
</StructureSection> | </StructureSection> | ||